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Effect of pore diffusion limitation on dextrin hydrolysis by immobilized glucoamylase
Author(s) -
Lee Douglas D.,
Lee Gene K.,
Reilly Peter J.,
Lee Yoon Y.
Publication year - 1980
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260220102
Subject(s) - dextrin , maltose , hydrolysis , chemistry , diffusion , substrate (aquarium) , chromatography , immobilized enzyme , enzyme , biochemistry , starch , thermodynamics , physics , oceanography , geology
Data reported here and previously indicate that when dextrin is hydrolyzed in the presence of immobilized glucoamylase, use of a larger average molecular weight substrate leads to lower overall rates of hydrolysis, while the maltose concentration during the bulk of the reaction and the maximum glucose concentration are lower than when the soluble form of the enzyme is employed under the same conditions. Computer simulation of the system demonstrated that all three observations were caused by pore diffusion limitation: the first by slow diffusion of substrate, the second by slow diffusion of intermediates, and the third by slow diffusion of glucose. Follow‐up experiments with glucoamylase immobilized to particles of different sizes confirmed this finding, as results with the smallest beads were identical to those with soluble glucoamylase.